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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1988-12-28
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pubmed:abstractText |
Canine liver alpha-L-fucosidase was purified to apparent homogeneity by affinity chromatography on agarose-epsilon-aminohexanoyl-fucopyranosylamine. It is composed of multiple forms of a common active subunit of 45-50 kDa, which can aggregate in different combinations to form polymers, predominantly dimers. Antiserum was raised against the purified enzyme. There is negligible residual alpha-L-fucosidase in the tissues of English springer spaniels with the lysosomal storage disease fucosidosis. Although no alpha-L-fucosidase protein was detected by Western blotting or by the purification procedure in the affected tissues, some enzymically inactive cross-reacting material was detected in both normal and affected tissues. This suggests that another protein without alpha-L-fucosidase activity was co-purified with the enzyme. Dog liver alpha-L-fucosidase was precipitated by goat anti-(human liver alpha-L-fucosidase) IgG, indicating homology between the enzymes in the two species. Two purified storage products isolated from the brain of a dog with fucosidosis were used as natural substrates for various preparations of canine liver alpha-L-fucosidase. Analysis of the digestion mixtures by t.l.c. and fast-atom-bombardment mass spectrometry suggests that canine alpha-L-fucosidase acts preferentially on the alpha-(1-3)-linked fucose at the non-reducing end and that removal of alpha-(1-6)-linked asparagine-linked N-acetylglucosamine is rate-limiting in the lysosomal catabolism of fucosylated N-linked glycans.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-21623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-240814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-26486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-2876234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-3084472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-3093228,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-3515668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-4050341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-4074382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-4411894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-4744832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-5154524,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-630552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-6419731,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-6463379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-6477509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-6661184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-6829151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-6880626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-7054178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-7072491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-7074133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-7341244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-7407197,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-7407198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-814895,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-845276,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-911860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-942051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3196299-98350
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
254
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
861-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:3196299-Animals,
pubmed-meshheading:3196299-Blotting, Western,
pubmed-meshheading:3196299-Chemical Precipitation,
pubmed-meshheading:3196299-Chromatography, Gel,
pubmed-meshheading:3196299-Chromatography, Thin Layer,
pubmed-meshheading:3196299-Dogs,
pubmed-meshheading:3196299-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3196299-Fucosidosis,
pubmed-meshheading:3196299-Isoenzymes,
pubmed-meshheading:3196299-Liver,
pubmed-meshheading:3196299-Tissue Distribution,
pubmed-meshheading:3196299-alpha-L-Fucosidase
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pubmed:year |
1988
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pubmed:articleTitle |
Canine alpha-L-fucosidase in relation to the enzymic defect and storage products in canine fucosidosis.
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pubmed:affiliation |
Department of Biochemistry, King's College London, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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